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Q6TGQ8

- OXLA_BOTMO

UniProt

Q6TGQ8 - OXLA_BOTMO

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops moojeni (Lance-headed viper) (Caissaca)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Phe>L-Tyr>L-Trp>L-Leu), thus producing hydrogen peroxide that may contribute to the toxicity of the venom. Exhibits diverse biological activities, such as edema, apoptosis of tumor cell lines, antibacterial activities against both Gram-positive and Gram-negative bacteria, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. It may also induce hemolysis, and have antiparasitic activities.2 Publications

    Catalytic activityi

    An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771FADBy similarity
    Binding sitei96 – 961SubstrateBy similarity
    Binding sitei229 – 2291SubstrateBy similarity
    Binding sitei267 – 2671FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei378 – 3781SubstrateBy similarity
    Binding sitei463 – 4631FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi49 – 502FADBy similarity
    Nucleotide bindingi69 – 702FADBy similarity
    Nucleotide bindingi93 – 964FADBy similarity
    Nucleotide bindingi470 – 4756FADBy similarity
    Nucleotide bindingi470 – 4712SubstrateBy similarity

    GO - Molecular functioni

    1. L-amino-acid oxidase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. defense response to Gram-negative bacterium Source: UniProtKB
    3. defense response to Gram-positive bacterium Source: UniProtKB
    4. hemolysis in other organism Source: UniProtKB-KW
    5. modulation of apoptotic process in other organism Source: UniProtKB

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation activating toxin, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    BmooLAAO-I
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiBothrops moojeni (Lance-headed viper) (Caissaca)
    Taxonomic identifieri98334 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 6›61 Publication
    Chaini7 – ›478›472L-amino-acid oxidasePRO_0000273565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi16 ↔ 179By similarity
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi337 ↔ 418By similarity

    Post-translational modificationi

    N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation.1 PublicationCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliQ6TGQ8.
    SMRiQ6TGQ8. Positions 9-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6TGQ8-1 [UniParc]FASTAAdd to Basket

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    RKAPCCADDR NPLEECFRET DYEEFLEIAK NGLSTTSNPK RVVIVGAGMS    50
    GLSAAYVLAN AGHQVTVLEA SERAGGRVKT YRNEKEGWYA NLGPMRLPEK 100
    HRIVREYIRK FDLQLNEFSQ ENENAWYFIK NIRKRVGEVN KDPGVLEYPV 150
    KPSEVGKSAG QLYEESLQKA VEELRRTNCS YMLNKYDTYS TKEYLLKEGN 200
    LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFAYEKRFD EIVGGMDKLP 250
    TSMYQAIQEK VHLNARVIKI QQDVKEVTVT YQTSEKETLS VTADYVIVCT 300
    TSRAARRIKF EPPLPPKKAH ALRSVHYRSG TKIFLTCTKK FWEDDGIHGG 350
    KSTTDLPSRF IYYPNHNFPN GVGVIIAYGI GDDANYFQAL DFEDCGDIVI 400
    NDLSLIHQLP KEEIQAICRP SMIQRWSLDK YAMGGITTFT PYQFQHFSEA 450
    LTAPVDRIYF AGEYTAQAHG WIDSTIKW 478
    Length:478
    Mass (Da):54,437
    Last modified:July 5, 2004 - v1
    Checksum:i555C159B029FB9CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti34 – 352ST → KS AA sequence (PubMed:17320169)Curated
    Non-terminal residuei478 – 4781

    Mass spectrometryi

    Molecular mass is 64889 Da from positions 7 - ?. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY398692 mRNA. Translation: AAR31183.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY398692 mRNA. Translation: AAR31183.1 .

    3D structure databases

    ProteinModelPortali Q6TGQ8.
    SMRi Q6TGQ8. Positions 9-477.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005729.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00757. AMINEOXDASEF.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling."
      Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O., Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V., Soares A.M.
      Biochem. Biophys. Res. Commun. 355:302-306(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Venom and Venom gland.
    2. Cited for: PROTEIN SEQUENCE OF 7-46, FUNCTION, SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY, CIRCULAR DICHROISM.
      Tissue: Venom.
    3. "Bothrops moojeni venom kills Leishmania spp. with hydrogen peroxide generated by its L-amino acid oxidase."
      Tempone A.G., Andrade H.F. Jr., Spencer P.J., Lourenco C.O., Rogero J.R., Nascimento N.
      Biochem. Biophys. Res. Commun. 280:620-624(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_BOTMO
    AccessioniPrimary (citable) accession number: Q6TGQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has parasiticidal activities against and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:11162565, PubMed:17292326).2 Publications

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3